HEADER LYASE 26-AUG-08 2JKB
TITLE CRYSTAL STRUCTURE OF STREPTOCOCCUS PNEUMONIAE NANB IN
TITLE 2 COMPLEX WITH 2,7-ANHYDRO-NEU5AC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIALIDASE B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 30-697;
COMPND 5 SYNONYM: NEURAMINIDASE B, NANB;
COMPND 6 EC: 4.2.2.15;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;
SOURCE 3 ORGANISM_TAXID: 170187;
SOURCE 4 STRAIN: TIGR4;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS INTRAMOLECULAR TRANS-SIALIDASE, LYASE, GLYCOSIDASE,
KEYWDS 2 NEURAMINIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.GUT,S.J.KING,M.A.WALSH
REVDAT 3 24-FEB-09 2JKB 1 VERSN
REVDAT 2 11-NOV-08 2JKB 1 JRNL REMARK
REVDAT 1 16-SEP-08 2JKB 0
JRNL AUTH H.GUT,S.J.KING,M.A.WALSH
JRNL TITL STRUCTURAL AND FUNCTIONAL STUDIES OF STREPTOCOCCUS
JRNL TITL 2 PNEUMONIAE NEURAMINIDASE B: AN INTRAMOLECULAR
JRNL TITL 3 TRANS-SIALIDASE.
JRNL REF FEBS LETT. V. 582 3348 2008
JRNL REFN ISSN 0014-5793
JRNL PMID 18775704
JRNL DOI 10.1016/J.FEBSLET.2008.08.026
REMARK 2
REMARK 2 RESOLUTION. 1.54 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.93
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 105364
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.500
REMARK 3 FREE R VALUE TEST SET COUNT : 2677
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.54
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.58
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6299
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 157
REMARK 3 BIN FREE R VALUE : 0.2590
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5439
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 1024
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 12.31
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : 0.03000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.073
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.073
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.047
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.258
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5616 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3785 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7631 ; 1.344 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9281 ; 0.803 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 716 ; 6.919 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 262 ;35.570 ;25.153
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 977 ;11.123 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;13.412 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 826 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6417 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1134 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 967 ; 0.190 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4044 ; 0.194 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2775 ; 0.176 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 3063 ; 0.082 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 769 ; 0.137 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 15 ; 0.226 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 51 ; 0.315 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 71 ; 0.157 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4467 ; 0.984 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5599 ; 1.102 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2591 ; 1.912 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2032 ; 2.555 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2JKB COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-AUG-08.
REMARK 100 THE PDBE ID CODE IS EBI-37278.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM14
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL CUT
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONICS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL2000
REMARK 200 DATA SCALING SOFTWARE : HKL2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 108114
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.54
REMARK 200 RESOLUTION RANGE LOW (A) : 25.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 3.6
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.30
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.0
REMARK 200 R MERGE FOR SHELL (I) : 0.35
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.60
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: HOMOLOGY MODEL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.7
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 6000, 200 MM TRIS PH
REMARK 280 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 38.35950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.03950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.37300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.03950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.35950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.37300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 HIS A 15
REMARK 465 HIS A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 SER A 19
REMARK 465 SER A 20
REMARK 465 GLY A 21
REMARK 465 LEU A 22
REMARK 465 GLU A 23
REMARK 465 VAL A 24
REMARK 465 LEU A 25
REMARK 465 PHE A 26
REMARK 465 GLN A 27
REMARK 465 GLY A 28
REMARK 465 PRO A 29
REMARK 465 ASN A 30
REMARK 465 GLU A 31
REMARK 465 LEU A 32
REMARK 465 ASN A 33
REMARK 465 TYR A 34
REMARK 465 GLY A 35
REMARK 465 GLN A 36
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 2222 - O HOH A 2940 2.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 262 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 51 63.99 -113.65
REMARK 500 ALA A 78 89.52 -153.57
REMARK 500 LYS A 80 57.08 -142.25
REMARK 500 GLN A 240 18.22 59.68
REMARK 500 ILE A 246 61.84 67.06
REMARK 500 SER A 273 -171.45 -171.82
REMARK 500 ASP A 327 88.71 68.56
REMARK 500 PRO A 534 40.89 -86.16
REMARK 500 TYR A 651 119.56 -160.45
REMARK 500 ALA A 652 -120.42 -125.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ILE A 365 ASN A 366 -39.37
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SKD A1698
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1699
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1704
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VW0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM
REMARK 900 STREPTOCOCCUS PNEUMONIAE
REMARK 900 RELATED ID: 2VW1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM
REMARK 900 STREPTOCOCCUS PNEUMONIAE
REMARK 900 RELATED ID: 2VW2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE NANB SIALIDASE FROM
REMARK 900 STREPTOCOCCUS PNEUMONIAE
DBREF 2JKB A 12 29 PDB 2JKB 2JKB 12 29
DBREF 2JKB A 30 697 UNP Q54727 NANB_STRPN 30 697
SEQRES 1 A 686 ALA HIS HIS HIS HIS HIS HIS SER SER GLY LEU GLU VAL
SEQRES 2 A 686 LEU PHE GLN GLY PRO ASN GLU LEU ASN TYR GLY GLN LEU
SEQRES 3 A 686 SER ILE SER PRO ILE PHE GLN GLY GLY SER TYR GLN LEU
SEQRES 4 A 686 ASN ASN LYS SER ILE ASP ILE SER SER LEU LEU LEU ASP
SEQRES 5 A 686 LYS LEU SER GLY GLU SER GLN THR VAL VAL MET LYS PHE
SEQRES 6 A 686 LYS ALA ASP LYS PRO ASN SER LEU GLN ALA LEU PHE GLY
SEQRES 7 A 686 LEU SER ASN SER LYS ALA GLY PHE LYS ASN ASN TYR PHE
SEQRES 8 A 686 SER ILE PHE MET ARG ASP SER GLY GLU ILE GLY VAL GLU
SEQRES 9 A 686 ILE ARG ASP ALA GLN LYS GLY ILE ASN TYR LEU PHE SER
SEQRES 10 A 686 ARG PRO ALA SER LEU TRP GLY LYS HIS LYS GLY GLN ALA
SEQRES 11 A 686 VAL GLU ASN THR LEU VAL PHE VAL SER ASP SER LYS ASP
SEQRES 12 A 686 LYS THR TYR THR MET TYR VAL ASN GLY ILE GLU VAL PHE
SEQRES 13 A 686 SER GLU THR VAL ASP THR PHE LEU PRO ILE SER ASN ILE
SEQRES 14 A 686 ASN GLY ILE ASP LYS ALA THR LEU GLY ALA VAL ASN ARG
SEQRES 15 A 686 GLU GLY LYS GLU HIS TYR LEU ALA LYS GLY SER ILE ASP
SEQRES 16 A 686 GLU ILE SER LEU PHE ASN LYS ALA ILE SER ASP GLN GLU
SEQRES 17 A 686 VAL SER THR ILE PRO LEU SER ASN PRO PHE GLN LEU ILE
SEQRES 18 A 686 PHE GLN SER GLY ASP SER THR GLN ALA ASN TYR PHE ARG
SEQRES 19 A 686 ILE PRO THR LEU TYR THR LEU SER SER GLY ARG VAL LEU
SEQRES 20 A 686 SER SER ILE ASP ALA ARG TYR GLY GLY THR HIS ASP SER
SEQRES 21 A 686 LYS SER LYS ILE ASN ILE ALA THR SER TYR SER ASP ASP
SEQRES 22 A 686 ASN GLY LYS THR TRP SER GLU PRO ILE PHE ALA MET LYS
SEQRES 23 A 686 PHE ASN ASP TYR GLU GLU GLN LEU VAL TYR TRP PRO ARG
SEQRES 24 A 686 ASP ASN LYS LEU LYS ASN SER GLN ILE SER GLY SER ALA
SEQRES 25 A 686 SER PHE ILE ASP SER SER ILE VAL GLU ASP LYS LYS SER
SEQRES 26 A 686 GLY LYS THR ILE LEU LEU ALA ASP VAL MET PRO ALA GLY
SEQRES 27 A 686 ILE GLY ASN ASN ASN ALA ASN LYS ALA ASP SER GLY PHE
SEQRES 28 A 686 LYS GLU ILE ASN GLY HIS TYR TYR LEU LYS LEU LYS LYS
SEQRES 29 A 686 ASN GLY ASP ASN ASP PHE ARG TYR THR VAL ARG GLU ASN
SEQRES 30 A 686 GLY VAL VAL TYR ASN GLU THR THR ASN LYS PRO THR ASN
SEQRES 31 A 686 TYR THR ILE ASN ASP LYS TYR GLU VAL LEU GLU GLY GLY
SEQRES 32 A 686 LYS SER LEU THR VAL GLU GLN TYR SER VAL ASP PHE ASP
SEQRES 33 A 686 SER GLY SER LEU ARG GLU ARG HIS ASN GLY LYS GLN VAL
SEQRES 34 A 686 PRO MET ASN VAL PHE TYR LYS ASP SER LEU PHE LYS VAL
SEQRES 35 A 686 THR PRO THR ASN TYR ILE ALA MET THR THR SER GLN ASN
SEQRES 36 A 686 ARG GLY GLU SER TRP GLU GLN PHE LYS LEU LEU PRO PRO
SEQRES 37 A 686 PHE LEU GLY GLU LYS HIS ASN GLY THR TYR LEU CYS PRO
SEQRES 38 A 686 GLY GLN GLY LEU ALA LEU LYS SER SER ASN ARG LEU ILE
SEQRES 39 A 686 PHE ALA THR TYR THR SER GLY GLU LEU THR TYR LEU ILE
SEQRES 40 A 686 SER ASP ASP SER GLY GLN THR TRP LYS LYS SER SER ALA
SEQRES 41 A 686 SER ILE PRO PHE LYS ASN ALA THR ALA GLU ALA GLN MET
SEQRES 42 A 686 VAL GLU LEU ARG ASP GLY VAL ILE ARG THR PHE PHE ARG
SEQRES 43 A 686 THR THR THR GLY LYS ILE ALA TYR MET THR SER ARG ASP
SEQRES 44 A 686 SER GLY GLU THR TRP SER LYS VAL SER TYR ILE ASP GLY
SEQRES 45 A 686 ILE GLN GLN THR SER TYR GLY THR GLN VAL SER ALA ILE
SEQRES 46 A 686 LYS TYR SER GLN LEU ILE ASP GLY LYS GLU ALA VAL ILE
SEQRES 47 A 686 LEU SER THR PRO ASN SER ARG SER GLY ARG LYS GLY GLY
SEQRES 48 A 686 GLN LEU VAL VAL GLY LEU VAL ASN LYS GLU ASP ASP SER
SEQRES 49 A 686 ILE ASP TRP LYS TYR HIS TYR ASP ILE ASP LEU PRO SER
SEQRES 50 A 686 TYR GLY TYR ALA TYR SER ALA ILE THR GLU LEU PRO ASN
SEQRES 51 A 686 HIS HIS ILE GLY VAL LEU PHE GLU LYS TYR ASP SER TRP
SEQRES 52 A 686 SER ARG ASN GLU LEU HIS LEU SER ASN VAL VAL GLN TYR
SEQRES 53 A 686 ILE ASP LEU GLU ILE ASN ASP LEU THR LYS
HET SKD A1698 20
HET EDO A1699 4
HET EDO A1700 4
HET EDO A1701 4
HET EDO A1702 4
HET EDO A1703 4
HET EDO A1704 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SKD 2-ACETYLAMINO-7-(1,2-DIHYDROXY-ETHYL)-3-
HETNAM 2 SKD HYDROXY-6,8-DIOXA-BICYCLO[3.2.1]OCTANE-5-
HETNAM 3 SKD CARBOXYLIC ACID
FORMUL 2 EDO 6(C2 H6 O2)
FORMUL 3 SKD C11 H17 N O8
FORMUL 4 HOH *1024(H2 O1)
HELIX 1 1 ILE A 57 LEU A 62 1 6
HELIX 2 2 ASP A 63 LEU A 65 5 3
HELIX 3 3 PRO A 176 ILE A 180 5 5
HELIX 4 4 SER A 216 THR A 222 1 7
HELIX 5 5 GLU A 691 THR A 696 1 6
SHEET 1 AA 6 PHE A 43 ASN A 51 0
SHEET 2 AA 6 LYS A 202 PHE A 211 -1 O GLY A 203 N LEU A 50
SHEET 3 AA 6 GLN A 70 LYS A 77 -1 O THR A 71 N PHE A 211
SHEET 4 AA 6 ASN A 144 ASP A 151 -1 O ASN A 144 N PHE A 76
SHEET 5 AA 6 THR A 156 VAL A 161 -1 O THR A 156 N ASP A 151
SHEET 6 AA 6 ILE A 164 THR A 170 -1 O ILE A 164 N VAL A 161
SHEET 1 AB 6 ILE A 55 ASP A 56 0
SHEET 2 AB 6 LYS A 185 LEU A 188 -1 O LEU A 188 N ILE A 55
SHEET 3 AB 6 LEU A 84 SER A 91 -1 O GLY A 89 N THR A 187
SHEET 4 AB 6 TYR A 101 ARG A 107 -1 O PHE A 102 N LEU A 90
SHEET 5 AB 6 ILE A 112 ASP A 118 -1 O GLY A 113 N PHE A 105
SHEET 6 AB 6 ILE A 123 ARG A 129 -1 O ILE A 123 N ASP A 118
SHEET 1 AC 2 LYS A 136 HIS A 137 0
SHEET 2 AC 2 GLN A 140 ALA A 141 -1 O GLN A 140 N HIS A 137
SHEET 1 AD 2 VAL A 191 ARG A 193 0
SHEET 2 AD 2 LYS A 196 HIS A 198 -1 O LYS A 196 N ARG A 193
SHEET 1 AE 3 TYR A 243 ARG A 245 0
SHEET 2 AE 3 VAL A 257 ARG A 264 -1 O ASP A 262 N ARG A 245
SHEET 3 AE 3 TYR A 250 THR A 251 -1 O TYR A 250 N LEU A 258
SHEET 1 AF 4 TYR A 243 ARG A 245 0
SHEET 2 AF 4 VAL A 257 ARG A 264 -1 O ASP A 262 N ARG A 245
SHEET 3 AF 4 ILE A 275 SER A 282 -1 O ASN A 276 N ALA A 263
SHEET 4 AF 4 ILE A 293 MET A 296 -1 O ILE A 293 N THR A 279
SHEET 1 AG 5 LYS A 475 LEU A 476 0
SHEET 2 AG 5 TYR A 458 SER A 464 -1 O MET A 461 N LYS A 475
SHEET 3 AG 5 THR A 339 MET A 346 -1 O THR A 339 N SER A 464
SHEET 4 AG 5 SER A 324 GLU A 332 -1 O SER A 324 N MET A 346
SHEET 5 AG 5 GLY A 493 GLN A 494 1 O GLY A 493 N ILE A 330
SHEET 1 AH 7 PHE A 362 GLU A 364 0
SHEET 2 AH 7 TYR A 369 LYS A 375 -1 O TYR A 370 N LYS A 363
SHEET 3 AH 7 TYR A 383 VAL A 385 -1 O TYR A 383 N LEU A 373
SHEET 4 AH 7 VAL A 390 ASN A 393 -1 O TYR A 392 N THR A 384
SHEET 5 AH 7 LYS A 398 ILE A 404 -1 O LYS A 398 N ASN A 393
SHEET 6 AH 7 VAL A 410 GLU A 412 -1 O LEU A 411 N THR A 403
SHEET 7 AH 7 LYS A 415 SER A 416 -1 O LYS A 415 N GLU A 412
SHEET 1 AI 3 PHE A 362 GLU A 364 0
SHEET 2 AI 3 TYR A 369 LYS A 375 -1 O TYR A 370 N LYS A 363
SHEET 3 AI 3 PHE A 451 LYS A 452 -1 O LYS A 452 N LYS A 374
SHEET 1 AJ 2 THR A 418 ASP A 425 0
SHEET 2 AJ 2 ARG A 432 PRO A 441 -1 O ARG A 432 N ASP A 425
SHEET 1 AK 3 TYR A 489 LEU A 490 0
SHEET 2 AK 3 LEU A 504 THR A 510 -1 O TYR A 509 N TYR A 489
SHEET 3 AK 3 LEU A 496 ALA A 497 -1 O LEU A 496 N ILE A 505
SHEET 1 AL 4 TYR A 489 LEU A 490 0
SHEET 2 AL 4 LEU A 504 THR A 510 -1 O TYR A 509 N TYR A 489
SHEET 3 AL 4 GLU A 513 SER A 519 -1 O GLU A 513 N THR A 510
SHEET 4 AL 4 LYS A 527 SER A 532 -1 O LYS A 527 N ILE A 518
SHEET 1 AM 4 ALA A 542 ARG A 548 0
SHEET 2 AM 4 VAL A 551 PHE A 556 -1 O VAL A 551 N LEU A 547
SHEET 3 AM 4 ALA A 564 SER A 568 -1 O ALA A 564 N PHE A 556
SHEET 4 AM 4 SER A 579 TYR A 580 -1 O SER A 579 N TYR A 565
SHEET 1 AN 4 SER A 594 ILE A 602 0
SHEET 2 AN 4 LYS A 605 PRO A 613 -1 O LYS A 605 N ILE A 602
SHEET 3 AN 4 GLY A 622 VAL A 629 -1 O GLN A 623 N THR A 612
SHEET 4 AN 4 ILE A 636 ASP A 643 -1 O ASP A 637 N LEU A 628
SHEET 1 AO 3 SER A 654 GLU A 658 0
SHEET 2 AO 3 ILE A 664 GLU A 669 -1 O GLY A 665 N THR A 657
SHEET 3 AO 3 VAL A 685 LEU A 690 -1 O GLN A 686 N PHE A 668
CISPEP 1 SER A 271 LYS A 272 0 2.64
SITE 1 AC1 17 ARG A 245 ILE A 246 ARG A 264 ASP A 270
SITE 2 AC1 17 ILE A 326 ASP A 327 ASP A 344 ASN A 352
SITE 3 AC1 17 THR A 539 GLU A 541 ARG A 557 ARG A 619
SITE 4 AC1 17 TYR A 653 TRP A 674 HOH A2457 HOH A3012
SITE 5 AC1 17 HOH A3013
SITE 1 AC2 7 LEU A 84 SER A 103 GLU A 115 TYR A 199
SITE 2 AC2 7 LYS A 335 HOH A3014 HOH A3015
SITE 1 AC3 6 TYR A 458 ILE A 459 LEU A 477 PRO A 478
SITE 2 AC3 6 PHE A 480 HOH A3016
SITE 1 AC4 10 VAL A 385 ILE A 404 ASN A 405 ASP A 406
SITE 2 AC4 10 TYR A 408 LYS A 475 HOH A2629 HOH A3017
SITE 3 AC4 10 HOH A3018 HOH A3019
SITE 1 AC5 6 THR A 251 GLN A 494 ILE A 596 THR A 657
SITE 2 AC5 6 HOH A2956 HOH A3020
SITE 1 AC6 6 SER A 617 LYS A 620 SER A 648 HOH A2911
SITE 2 AC6 6 HOH A3021 HOH A3022
SITE 1 AC7 8 ARG A 256 ASN A 466 ARG A 467 GLU A 469
SITE 2 AC7 8 SER A 617 HOH A2444 HOH A3023 HOH A3024
CRYST1 76.719 82.746 118.079 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013035 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012085 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008469 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
